Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0016020 | cellular_component | membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
A | 0046689 | biological_process | response to mercury ion |
A | 0055085 | biological_process | transmembrane transport |
A | 0140359 | molecular_function | ABC-type transporter activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0016020 | cellular_component | membrane |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
B | 0046689 | biological_process | response to mercury ion |
B | 0055085 | biological_process | transmembrane transport |
B | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE LDA A 701 |
Chain | Residue |
A | THR113 |
A | LEU116 |
A | GLY147 |
A | THR148 |
A | ASP331 |
A | GLU334 |
A | MSE335 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LDA A 702 |
Chain | Residue |
B | ILE144 |
B | LDA702 |
A | ASP217 |
A | TYR247 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 704 |
Chain | Residue |
A | ARG114 |
A | HIS115 |
B | ARG252 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 705 |
Chain | Residue |
A | SER396 |
A | GLY399 |
A | LYS400 |
A | SER401 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 706 |
Chain | Residue |
A | ARG206 |
A | ARG210 |
A | MSE320 |
A | ARG323 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDA B 701 |
Chain | Residue |
A | VAL120 |
A | LEU124 |
A | THR148 |
B | ASP217 |
B | TYR247 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE LDA B 702 |
Chain | Residue |
A | LDA702 |
B | THR113 |
B | GLY147 |
B | ASP331 |
B | GLU334 |
B | MSE335 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 704 |
Chain | Residue |
B | SER396 |
B | GLY399 |
B | LYS400 |
B | SER401 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 B 705 |
Chain | Residue |
A | ARG252 |
B | ARG114 |
B | HIS115 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 706 |
Chain | Residue |
B | ARG206 |
B | ARG210 |
B | MSE320 |
B | ARG323 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARTL |
Chain | Residue | Details |
A | LEU498-LEU512 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | MSE1-ARG38 | |
A | GLU106-MSE154 | |
A | THR203-GLY266 | |
A | ARG323-GLU608 | |
B | MSE1-ARG38 | |
B | GLU106-MSE154 | |
B | THR203-GLY266 | |
B | ARG323-GLU608 | |
site_id | SWS_FT_FI2 |
Number of Residues | 254 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
A | VAL39-TYR60 | |
B | PHE180-ILE202 | |
B | LEU267-ALA285 | |
B | LEU301-TYR322 | |
A | PHE83-PHE105 | |
A | LEU155-LEU178 | |
A | PHE180-ILE202 | |
A | LEU267-ALA285 | |
A | LEU301-TYR322 | |
B | VAL39-TYR60 | |
B | PHE83-PHE105 | |
B | LEU155-LEU178 | |
Chain | Residue | Details |
A | LYS61-ALA82 | |
A | ASN179 | |
A | TRP286-ASP300 | |
B | LYS61-ALA82 | |
B | ASN179 | |
B | TRP286-ASP300 | |
Chain | Residue | Details |
A | ARG206 | |
B | ARG206 | |
Chain | Residue | Details |
A | ASN269 | |
A | ASP316 | |
B | ASN269 | |
B | ASP316 | |
Chain | Residue | Details |
A | TYR370 | |
B | TYR370 | |
Chain | Residue | Details |
A | GLY394 | |
B | GLY394 | |